(Q46256041)

20 December 2017

title

N-glycosylation at the conserved sites ensures the expression of properly folded functional ACh receptors (English)

1 reference

20 December 2017

1 reference

Gehle VM

1

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20 December 2017

Walcott EC

series ordinal

2

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20 December 2017

Nishizaki T

series ordinal

3

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20 December 2017

Sumikawa K

series ordinal

4

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20 December 2017

publication date

1 May 1997

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20 December 2017

published in

Molecular Brain Research

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20 December 2017

volume

45

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20 December 2017

issue

2

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20 December 2017

page(s)

219-229

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20 December 2017

In vitro synthesis, glycosylation, and membrane insertion of the four subunits of Torpedo acetylcholine receptor

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7 January 2021

Molecular basis of the two nonequivalent ligand binding sites of the muscle nicotinic acetylcholine receptor

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Assembly intermediates of the mouse muscle nicotinic acetylcholine receptor in stably transfected fibroblasts

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The nicotinic acetylcholine receptor: structure and autoimmune pathology

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Functional architecture of the nicotinic acetylcholine receptor: a prototype of ligand-gated ion channels

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Monoclonal antibodies specific for each of the two toxin-binding sites of Torpedo acetylcholine receptor

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Analysis of subunit assembly of the Na-K-ATPase

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7 January 2021

Role of two acetylcholine receptor subunit domains in homomer formation and intersubunit recognition, as revealed by alpha 3 and alpha 7 subunit chimeras

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7 January 2021

Site-directed mutagenesis of the conserved N-glycosylation site on the nicotinic acetylcholine receptor subunits

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7 January 2021

Role of the Endoplasmic Reticulum Chaperone Calnexin in Subunit Folding and Assembly of Nicotinic Acetylcholine Receptors

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7 January 2021

Acetylcholine receptor assembly: subunit folding and oligomerization occur sequentially

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7 January 2021

Assembly of the mammalian muscle acetylcholine receptor in transfected COS cells

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7 January 2021

Assessment of the number of free cysteines and isolation and identification of cystine-containing peptides from acetylcholine receptor

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7 January 2021

Assembly in vivo of mouse muscle acetylcholine receptor: identification of an alpha subunit species that may be an assembly intermediate

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7 January 2021

Synthesis and assembly of acetylcholine receptor, a multisubunit membrane glycoprotein

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7 January 2021

Carbohydrate structures of acetylcholine receptor from Torpedo californica and distribution of oligosaccharides among the subunits

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7 January 2021

Molecular structure of the nicotinic acetylcholine receptor

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7 January 2021

Desensitization of the nicotinic acetylcholine receptor: molecular mechanisms and effect of modulators

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7 January 2021

Analysis of early events in acetylcholine receptor assembly

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7 January 2021

Efficiency of acetylcholine receptor subunit assembly and its regulation by cAMP

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7 January 2021

Assembly of Torpedo acetylcholine receptors in Xenopus oocytes

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7 January 2021

Role of acetylcholine receptor subunits in gating of the channel

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7 January 2021

Sequences on the N-terminus of ACh receptor subunits regulate their assembly

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7 January 2021

Assembly and N-glycosylation of all ACh receptor subunits are required for their efficient insertion into plasma membranes

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7 January 2021

The amino acid residues 1-128 in the alpha subunit of the nicotinic acetylcholine receptor contain assembly signals.

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7 January 2021

The N-terminal domains of acetylcholine receptor subunits contain recognition signals for the initial steps of receptor assembly

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7 January 2021

Mouse-Torpedo hybrid acetylcholine receptors: functional homology does not equal sequence homology

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7 January 2021

Extracellular domains mediating epsilon subunit interactions of muscle acetylcholine receptor

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7 January 2021

A sequence in the main cytoplasmic loop of the alpha subunit is required for assembly of mouse muscle nicotinic acetylcholine receptor

1 reference

https://api.crossref.org/works/10.1016%2FS0169-328X%2896%2900256-2

7 January 2021

10.1016/S0169-328X(96)00256-2

Identifiers

DOI

1 reference

20 December 2017

1 reference

20 December 2017